Linked Life Data

3048416

Source:http://linkedlifedata.com/resource/pubmed/id/3048416

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1988-11-23
pubmed:abstractText
Two secretory glycoproteins of Saccharomyces cerevisiae, a soluble thiamin-binding protein and a thiamin-repressible acid phosphatase, were shown to be repressed to a similar extent by excess thiamin in the growth medium. Thiamin-repressible acid phosphatase was co-purified throughout the purification of the soluble thiamin-binding protein. Purified and deglycosylated soluble thiamin-binding proteins exhibited both thiamin-binding and acid phosphatase activity on non-denaturing polyacrylamide gel electrophoresis. Heat treatment of the purified soluble thiamin-binding protein caused a decrease in both activities with a similar inactivation profile. Furthermore, two thiamin-repressible acid phosphatase-defective mutants isolated had no and decreased soluble thiamin-binding activity, respectively. From the results, it was concluded that the soluble thiamin-binding protein is identical to the thiamin-repressible acid phosphatase in S. cerevisiae.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
967
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
49-55
pubmed:dateRevised
2009-7-21
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Identity of soluble thiamin-binding protein with thiamin-repressible acid phosphatase in Saccharomyces cerevisiae.
pubmed:affiliation
Department of Biochemistry, Kyoto Prefectural University of Medicine, Japan.
pubmed:publicationType
Journal Article